Chloroplast transit peptides: Structure, function and evolution

Trends in Cell Biology

Volumn 10, Issue 10, 2000, Pages 440-447

  Bruce, Barry D ^a,b  

^a UNIVERSITY OF TENNESSEE   (United States)

^b OAK RIDGE NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; PROTEIN PRECURSOR; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; CHLOROPLAST; EVOLUTION; GENE SEQUENCE; GENETIC ANALYSIS; PLANT; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN LIPID INTERACTION; PROTEIN PROTEIN INTERACTION; REVIEW;

BIOLOGICAL TRANSPORT; CHLOROPLASTS; EVOLUTION, MOLECULAR; PLANT PROTEINS; PROTEIN SORTING SIGNALS;

EID: 0034308219     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0962-8924(00)01833-X     Document Type: Review

References (66)

1. Weeden N.F. Genetic and biochemical implications of the endosymbiotic origin of the chloroplast. J. Mol. Evol. 17:1981;133-139.
2. Kaneko T.et al. Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res. 3:1996;109-136.
3. Chua N.H., Schmidt G.W. Post-translational transport into intact chloroplasts of a precursor to the small subunit of ribulose-1,5-bisphosphate carboxylase. Proc. Natl. Acad. Sci. U. S. A. 75:1978;6110-6114.
4. Highfield P.E., Ellis R.J. Synthesis and transport of the small of ribulose bisphosphate carboxylase. Nature. 271:1978;420-424.
5. Douglas S.E. Plastid evolution: origins, diversity, trends. Curr. Opin. Genet. Dev. 8:1998;655-661.
6. Gray M.W. Evolution of organellar genomes. Curr. Opin. Genet. Dev. 9:1999;678-687.
7. Martin W., Herrmann R.G. Gene transfer from organelles to the nucleus: how much, what happens, and Why? Plant Physiol. 118:1998;9-17.
8. Keegstra K., Cline K. Protein import and routing systems of chloroplasts. Plant Cell. 11:1999;557-570.
9. Chen X., Schnell D.J. Protein import into chloroplasts. Trends Cell Biol. 9:1999;222-227.
10. von Heijne G.et al. CHLPEP- A database of chloroplast transit peptides. Plant Mol. Biol. Rep. 9:1991;104-126.
11. Emanuelsson O.et al. ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites. Protein Sci. 8:1999;978-984.
12. Lin X.et al. Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana. Nature. 402:1999;761-768.
13. Mayer K.et al. Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana. Nature. 402:1999;769-777.
14. Bruce B.D. The role of lipids in plastid protein transport. Plant Mol. Biol. 38:1998;223-246.
15. Wienk H.L.et al. The structural flexibility of the preferredoxin transit peptide. FEBS Lett. 453:1999;318-326.
16. Krimm I.et al. A coil-helix instead of a helix-coil motif can be induced in a chloroplast transit peptide from Chlamydomonas reinhardtii. 265:1999;171-180.
17. von Heijne G., Nishikawa K. Chloroplast transit peptides. The perfect random coil? FEBS Lett. 278:1991;1-3.
18. Endo T.et al. The chloroplast-targeting domain of plastocyanin transit peptide can form a helical structure but does not have a high affinity for lipid bilayers. Eur. J. Biochem. 207:1992;671-675.
19. Buck M. Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins. Q. Rev. Biophys. 31:1998;297-355.
20. Lancelin J.M.et al. NMR structures of ferredoxin chloroplastic transit peptide from Chlamydomonas reinhardtii promoted by trifluoroethanol in aqueous solution. FEBS Lett. 343:1994;261-266.
21. Wienk H.L.et al. Structure, dynamics, and insertion of a chloroplast targeting peptide in mixed micelles. Biochemistry. 39:2000;8219-8227.
22. Pilon M.et al. Functional domains of the ferredoxin transit sequence involved in chloroplast import. J. Biol. Chem. 270:1995;3882-3893.
23. Bolter B.et al. A protein import receptor in pea chloroplasts, Toc86, is only a proteolytic fragment of a larger polypeptide. FEBS Lett. 441:1998;59-62.
24. Bauer J.et al. The major protein import receptor of plastids is essential for chloroplast biogenesis. Nature. 403:2000;203-207.
25. Karlin-Neumann G.A., Tobin E.M. Transit peptides of nuclear-encoded chloroplast proteins share a common amino acid framework. EMBO J. 5:1986;9-13.
26. von Heijne G.et al. Domain structure of mitochondrial and chloroplast targeting peptides. Eur. J. Biochem. 180:1989;535-545.
27. Claros M.G.et al. Prediction of N-terminal protein sorting signals. Curr. Opin. Struct. Biol. 7:1997;394-398.
28. Endo T., Schatz G. Latent membrane perturbation activity of a mitochondrial precursor protein is exposed by unfolding [published erratum appears in EMBO J. (1988) 7, 1915]. EMBO J. 7:1988;1153-1158.
29. Reitveld A.G.et al. Non-bilayer lipids are required for efficient protein transport across the plasma membrane of E. coli. EMBO J. 14:1995;5506-5513.
30. van't Hof R.et al. Lipid-peptide interactions between fragments of the transit peptide of ribulose-1,5-bisphosphate carboxylase/oxygenase and chloroplast membrane lipids. FEBS Lett. 291:1991;350-354.
31. Pinnaduwage P., Bruce B.D. In vitro interaction between a chloroplast transit peptide and chloroplast outer envelope lipids is sequence-specific and lipid class-dependent. J. Biol. Chem. 271:1996;32907-32915.
32. van't Hof R.et al. The transit sequence mediates the specific interaction of the precursor of ferredoxin with chloroplast envelope membrane lipids. J. Biol. Chem. 268:1993;4037-4042.
33. Douce R., Joyard J. Biochemistry and function of the plastid envelope. Annu. Rev. Cell Biol. 6:1990;173-216.
34. Dabney-Smith C.et al. The C terminus of a chloroplast precursor modulates its interaction with the translocation apparatus and PIRAC. J. Biol. Chem. 274:1999;32351-32359.
35. Perry S.E., Keegstra K. Envelope membrane proteins that interact with chloroplastic precursor proteins. Plant Cell. 6:1994;93-105.
36. Ma Y.et al. Two components of the chloroplast protein import apparatus, IAP86 and IAP75, interact with the transit sequence during the recognition and translocation of precursor proteins at the outer envelope. J. Cell Biol. 134:1996;315-327.
37. Rensink W.A.et al. The transit sequence of ferredoxin contains different domains for translocation across the outer and inner membrane of the chloroplast envelope. J. Biol. Chem. 275:2000;10265-10271.
38. Sveshnikova N.et al. Toc34 is a preprotein receptor regulated by GTP and phosphorylation. Proc. Natl. Acad. Sci. U. S. A. 97:2000;4973-4978.
39. Kessler F.et al. Identification of two GTP-binding proteins in the chloroplast protein import machinery. Science. 266:1994;1035-1039.
40. Seedorf M.et al. A constituent of the chloroplast import complex represents a new type of GTP-binding protein. Plant J. 7:1995;401-411.
41. Heins L.et al. The protein translocation apparatus of chloroplast envelopes. Trends Plant Sci. 3:1998;56-61.
42. Kindle K.L. Amino-terminal and hydrophobic regions of the Chlamydomonas reinhardtii plastocyanin transit peptide are required for efficient protein accumulation in vivo. Plant Mol. Biol. 38:1998;365-377.
43. Kindle K.L., Lawrence S.D. Transit peptide mutations that impair in vitro and in vivo chloroplast protein import do not affect accumulation of the gamma-subunit of chloroplast ATPase. Plant Physiol. 116:1998;1179-1190.
44. Rensink W.A.et al. Domains of a transit sequence required for in vivo import in Arabidopsis chloroplasts. Plant Physiol. 118:1998;691-699.
45. Lawrence S.D., Kindle K.L. Alterations in the Chlamydomonas plastocyanin transit peptide have distinct effects on in vitro import and in vivo protein accumulation. J. Biol. Chem. 272:1997;20357-20363.
46. Schatz G., Dobberstein B. Common principles of protein translocation across membranes. Science. 271:1996;1519-1526.
47. May T., Soll J. 14-3-3 proteins form a guidance complex with chloroplast precursor proteins in plants. Plant Cell. 12:2000;53-64.
48. Komiya T.et al. Binding of mitochondrial precursor proteins to the cytoplasmic domains of the import receptors Tom70 and Tom20 is determined by cytoplasmic chaperones. EMBO J. 16:1997;4267-4275.
49. Waegemann K., Soll J. Phosphorylation of the transit sequence of chloroplast precursor proteins. J. Biol. Chem. 271:1996;6545-6554.
50. Muslin A.J.et al. Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell. 84:1996;889-897.
51. Pilon M.et al. Kinetic analysis of translocation into isolated chloroplasts of the purified ferredoxin precursor. FEBS Lett. 302:1992;65-68.
52. Pilon M., Schekman R. Protein translocation: how Hsp70 pulls it off. Cell. 97:1999;679-682.
53. Marshall J.S.et al. Identification of heat shock protein hsp70 homologues in chloroplasts. Proc. Natl. Acad. Sci. U. S. A. 87:1990;374-378.
54. Ivey R.A., Bruce B.D. In vivo and in vitro interaction of DnaK and a chloroplast transit peptide. Cell Stress Chaperones. 5:2000;62-71.
55. Ivey R.A. 3rd et al. Identification of a hsp70 recognition domain within the rubisco small subunit transit peptide. Plant Physiol. 122:2000;1289-1300.
56. Stahl T.et al. Tic40, a new `old' subunit of the chloroplast protein import translocon. J. Biol. Chem. 274:1999;37467-37472.
57. Zhang X.P.et al. Interaction of mitochondrial presequences with DnaK and mitochondrial hsp70. J. Mol. Biol. 288:1999;177-190.
58. Bolter B.et al. Origin of a chloroplast protein importer. Proc. Natl. Acad. Sci. U. S. A. 95:1998;15831-15836.
59. Reumann S., Keegstra K. The endosymbiotic origin of the protein import machinery of chloroplastic envelope membranes. Trends Plant Sci. 4:1999;302-307.
60. Reumann S.et al. The evolutionary origin of the protein-translocating channel of chloroplastic envelope membranes: identification of a cyanobacterial homolog. Proc. Natl. Acad. Sci. U. S. A. 96:1999;784-789.
61. McFadden G.I. Endosymbiosis and evolution of the plant cell. Curr. Opin. Plant Biol. 2:1999;513-519.
62. de Souza S.J.et al. Intron positions correlate with module boundaries in ancient proteins. Proc. Natl. Acad. Sci. U. S. A. 93:1996;14632-14636.
63. Quigley F.et al. Intron conservation across the prokaryote-eukaryote boundary: structure of the nuclear gene for chloroplast glyceraldehyde-3-phosphate dehydrogenase from maize. Proc. Natl. Acad. Sci. U. S. A. 85:1988;2672-2676.
64. Gregerson R.G.et al. Genomic structure, expression and evolution of the alfalfa aspartate aminotransferase genes. Plant Mol. Biol. 25:1994;387-399.
65. Long M.et al. Exon shuffling and the origin of the mitochondrial targeting function in plant cytochrome c1 precursor. Proc. Natl. Acad. Sci. U. S. A. 93:1996;7727-7731.
66. Liaud M.F.et al. Differential intron loss and endosymbiotic transfer of chloroplast glyceraldehyde-3-phosphate dehydrogenase genes to the nucleus. Proc. Natl. Acad. Sci. U. S. A. 87:1990;8918-8922.